ID   ELA2A_HUMAN             Reviewed;         269 AA.
AC   P08217; Q14243;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   07-JUL-2009, entry version 92.
DE   RecName: Full=Elastase-2A;
DE            EC=3.4.21.71;
DE   Flags: Precursor;
GN   Name=ELA2A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88107669; PubMed=3427074; DOI=10.1021/bi00397a010;
RA   Fletcher T.S., Shen W.F., Largman C.;
RT   "Primary structure of human pancreatic elastase 2 determined by
RT   sequence analysis of the cloned mRNA.";
RL   Biochemistry 26:7256-7261(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87217962; PubMed=3646943;
RA   Kawashima I., Tani T., Shimoda K., Takiguchi Y.;
RT   "Characterization of pancreatic elastase II cDNAs: two elastase II
RT   mRNAs are expressed in human pancreas.";
RL   DNA 6:163-172(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   MEDLINE=88198076; PubMed=2834346;
RA   Shirasu Y., Yoshida H., Matsuki S., Takemura K., Ikeda N., Shimada Y.,
RA   Ozawa T., Mikayama T., Iijima H., Ishida A., Sato Y., Tamai Y.,
RA   Tanaka J., Ikenaga H.;
RT   "Molecular cloning and expression in Escherichia coli of a cDNA
RT   encoding human pancreatic elastase 2.";
RL   J. Biochem. 102:1555-1563(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 18-50, AND INTERACTION WITH CPA1.
RX   MEDLINE=90169111; PubMed=2307232; DOI=10.1016/0014-5793(90)80665-6;
RA   Moulard M., Michon T., Kerfelec B., Chapus C.;
RT   "Further studies on the human pancreatic binary complexes involving
RT   procarboxypeptidase A.";
RL   FEBS Lett. 261:179-183(1990).
CC   -!- FUNCTION: Acts upon elastin.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Leu-|-Xaa, Met-|-Xaa
CC       and Phe-|-Xaa. Hydrolyzes elastin.
CC   -!- SUBUNIT: Interacts with CPA1.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Pancreas.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   EMBL; M16631; AAA52374.1; -; mRNA.
DR   EMBL; M16652; AAA52380.1; -; mRNA.
DR   EMBL; D00236; BAA00165.1; -; mRNA.
DR   EMBL; AL512883; CAC42421.1; -; Genomic_DNA.
DR   EMBL; BC007031; AAH07031.1; -; mRNA.
DR   IPI; IPI00027722; -.
DR   PIR; B26823; B26823.
DR   RefSeq; NP_254275.1; -.
DR   UniGene; Hs.631866; -.
DR   HSSP; P08419; 1BRU.
DR   SMR; P08217; 29-269.
DR   MEROPS; S01.155; -.
DR   PRIDE; P08217; -.
DR   Ensembl; ENSG00000142615; Homo sapiens.
DR   GeneID; 63036; -.
DR   KEGG; hsa:63036; -.
DR   UCSC; uc001awk.1; human.
DR   GeneCards; GC01P015655; -.
DR   H-InvDB; HIX0000152; -.
DR   MIM; 609443; gene.
DR   HOVERGEN; P08217; -.
DR   BRENDA; 3.4.21.71; 247.
DR   NextBio; 65535; -.
DR   PMAP-CutDB; P08217; -.
DR   ArrayExpress; P08217; -.
DR   Bgee; P08217; -.
DR   GermOnline; ENSG00000142615; Homo sapiens.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Polymorphism; Protease; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL        1     16
FT   PROPEP       17     28       Activation peptide.
FT                                /FTId=PRO_0000027693.
FT   CHAIN        29    269       Elastase-2A.
FT                                /FTId=PRO_0000027694.
FT   DOMAIN       29    267       Peptidase S1.
FT   ACT_SITE     73     73       Charge relay system (By similarity).
FT   ACT_SITE    121    121       Charge relay system (By similarity).
FT   ACT_SITE    216    216       Charge relay system (By similarity).
FT   DISULFID     58     74       By similarity.
FT   DISULFID    155    222       By similarity.
FT   DISULFID    186    202       By similarity.
FT   DISULFID    212    243       By similarity.
FT   VARIANT     257    257       N -> S (in dbSNP:rs2303193).
FT                                /FTId=VAR_051837.
FT   CONFLICT    202    202       C -> V (in Ref. 3; BAA00165).
SQ   SEQUENCE   269 AA;  28888 MW;  A2E05143EFF4987C CRC64;
     MIRTLLLSTL VAGALSCGDP TYPPYVTRVV GGEEARPNSW PWQVSLQYSS NGKWYHTCGG
     SLIANSWVLT AAHCISSSRT YRVGLGRHNL YVAESGSLAV SVSKIVVHKD WNSNQISKGN
     DIALLKLANP VSLTDKIQLA CLPPAGTILP NNYPCYVTGW GRLQTNGAVP DVLQQGRLLV
     VDYATCSSSA WWGSSVKTSM ICAGGDGVIS SCNGDSGGPL NCQASDGRWQ VHGIVSFGSR
     LGCNYYHKPS VFTRVSNYID WINSVIANN
//